ID   L0A4I6_DEIPD            Unreviewed;       846 AA.
AC   L0A4I6;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00022419, ECO:0000256|HAMAP-Rule:MF_00595};
DE            Short=PEPC {ECO:0000256|HAMAP-Rule:MF_00595};
DE            Short=PEPCase {ECO:0000256|HAMAP-Rule:MF_00595};
DE            EC=4.1.1.31 {ECO:0000256|ARBA:ARBA00012305, ECO:0000256|HAMAP-Rule:MF_00595};
GN   Name=ppc {ECO:0000256|HAMAP-Rule:MF_00595};
GN   OrderedLocusNames=Deipe_3321 {ECO:0000313|EMBL:AFZ68761.1};
OS   Deinococcus peraridilitoris (strain DSM 19664 / LMG 22246 / CIP 109416 /
OS   KR-200).
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=937777 {ECO:0000313|EMBL:AFZ68761.1, ECO:0000313|Proteomes:UP000010467};
RN   [1] {ECO:0000313|Proteomes:UP000010467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19664 / LMG 22246 / CIP 109416 / KR-200
RC   {ECO:0000313|Proteomes:UP000010467};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Lu M.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA   Woyke T., Wu D., Pukall R., Steenblock K., Brambilla E., Klenk H.-P.,
RA   Eisen J.A.;
RT   "Complete sequence of chromosome of Deinococcus peraridilitoris DSM
RT   19664.";
RL   Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source
CC       for the tricarboxylic acid cycle. {ECO:0000256|ARBA:ARBA00003670,
CC       ECO:0000256|HAMAP-Rule:MF_00595}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=oxaloacetate + phosphate = hydrogencarbonate +
CC         phosphoenolpyruvate; Xref=Rhea:RHEA:28370, ChEBI:CHEBI:16452,
CC         ChEBI:CHEBI:17544, ChEBI:CHEBI:43474, ChEBI:CHEBI:58702; EC=4.1.1.31;
CC         Evidence={ECO:0000256|ARBA:ARBA00001071, ECO:0000256|HAMAP-
CC         Rule:MF_00595};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946, ECO:0000256|HAMAP-
CC         Rule:MF_00595};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00595}.
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC       {ECO:0000256|ARBA:ARBA00008346, ECO:0000256|HAMAP-Rule:MF_00595}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP003382; AFZ68761.1; -; Genomic_DNA.
DR   RefSeq; WP_015237059.1; NC_019793.1.
DR   AlphaFoldDB; L0A4I6; -.
DR   STRING; 937777.Deipe_3321; -.
DR   KEGG; dpd:Deipe_3321; -.
DR   PATRIC; fig|937777.3.peg.3336; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_0; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000010467; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-UniRule.
DR   GO; GO:0006107; P:oxaloacetate metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   HAMAP; MF_00595; PEPcase_type1; 1.
DR   InterPro; IPR021135; PEP_COase.
DR   InterPro; IPR022805; PEP_COase_bac/pln-type.
DR   InterPro; IPR018129; PEP_COase_Lys_AS.
DR   InterPro; IPR033129; PEPCASE_His_AS.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   PANTHER; PTHR30523; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   PANTHER; PTHR30523:SF6; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   Pfam; PF00311; PEPcase; 2.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   PROSITE; PS00781; PEPCASE_1; 1.
DR   PROSITE; PS00393; PEPCASE_2; 1.
PE   3: Inferred from homology;
KW   Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300, ECO:0000256|HAMAP-
KW   Rule:MF_00595};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00595};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00595};
KW   Pyruvate {ECO:0000313|EMBL:AFZ68761.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010467}.
FT   ACT_SITE        141
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        521
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   846 AA;  93958 MW;  58953D78F0DBA7F3 CRC64;
     MTDVRQNARQ GELRSDVSTL GRALGTVLRE QEGEAFFELV EQVRALVRDA RDAGRDAPLR
     DVLASASPQD AENLVRAFSW YFQLVNLAEE YERVRALRGR EGPRPQSLED ALVKLQARGW
     SAEKVEALSR SVELNLTFTA HPTEMRRRTT RTHLEEIARD LPNLNEEALA RITAHIEAMW
     GTLELRRLKP TVQDEVKAGL SYVRSIAQAL PRLSRDWRLA FERVYGRSPQ VRDAVSGKGV
     ELPLKFSSWM GGDRDGNPFV TPEATRDTLA LHAERARDQL LEVLARAFAY VSQQQQGQEP
     WRGEIQAIYD GVYDGVARGK DVDVVGRLEA LDGALRLAGQ RRSADELLGP ALTLARTFGR
     HLVSLDIREH SEVVGAAVSL LLREAGVENY ETLSETEKQQ VLRRELASRR PLWPAGEERP
     EALERTVGPI REVAHAVRAV GAGAFGRYVI SMAESVSDVL EPLLLAREVG FRVLPVPLFE
     TLDDLANGPG VIRELLALPE YRRVLQDDVQ EIMLGYSDSN KDAGFLAANW ALHEAQRNIA
     AVCREAGVTW RFFHGRGTSI GRGGGPAARA ILGQPGGTIG AGLRLTEQGE ALADKYSHPL
     LAHRNLEQAL HGLLLAAARD DELLPSDWTE ALSRGAAASV QAYRALVDHE DFLGFFEAVT
     PIHEIARLNI ASRPVRRPGA PTLHNLRAIP WVMSWTQNRA NLPGWYGLAE GLRAIGEGQA
     REMYREWPFF RAVLDNAQMS LAKSDLLIFD EYLRLAPVSA LASRIKEAYA ETVMRVEDAV
     GGPLLLHEPR LRTSIELRNP YVDPIHRLQV ELLQRARAQG GEMPEDMERA LLLTIQGIAA
     GMRNTG
//